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HEADER HYDROLASE(O-GLYCOSYL) 08-AUG-91 1NSB TITLE THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA TITLE 2 B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS; SOURCE 3 STRAIN: B/BEIJING/1/87 KEYWDS HYDROLASE(O-GLYCOSYL) EXPDTA X-RAY DIFFRACTION AUTHOR W.P.BURMEISTER,R.W.H.RUIGROK,S.CUSACK REVDAT 2 01-APR-03 1NSB 1 JRNL REVDAT 1 31-OCT-93 1NSB 0 JRNL AUTH W.P.BURMEISTER,R.W.RUIGROK,S.CUSACK JRNL TITL THE 2.2 A RESOLUTION CRYSTAL STRUCTURE OF JRNL TITL 2 INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH JRNL TITL 3 SIALIC ACID. JRNL REF EMBO J. V. 11 49 1992 JRNL REFN ASTM EMJODG UK ISSN 0261-4189 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH W.-P.BURMEISTER,R.S.DANIELS,S.DAYAN,J.GAGNON, REMARK 1 AUTH 2 S.CUSACK,R.W.H.RUIGROK REMARK 1 TITL SEQUENCE AND CRYSTALLIZATION OF INFLUENZA VIRUS REMARK 1 TITL 2 B(SLASH)BEIJING(SLASH)1(SLASH)87 NEURAMINIDASE REMARK 1 REF VIROLOGY V. 180 266 1991 REMARK 1 REFN ASTM VIRLAX US ISSN 0042-6822 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.148 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7469 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 57 REMARK 3 SOLVENT ATOMS : 1332 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.016 REMARK 3 BOND ANGLES (DEGREES) : 3.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NSB COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.95 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.26667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 148.53333 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 148.53333 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 74.26667 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 CA CA 3 LIES ON A SPECIAL POSITION. REMARK 375 HOH 1062 LIES ON A SPECIAL POSITION. REMARK 375 HOH 1821 LIES ON A SPECIAL POSITION. REMARK 375 HOH 1961 LIES ON A SPECIAL POSITION. DBREF 1NSB A 76 465 UNP P27907 NRAM_INBBE 76 465 DBREF 1NSB B 76 465 UNP P27907 NRAM_INBBE 76 465 SEQRES 1 A 390 GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SEQRES 2 A 390 SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG SEQRES 3 A 390 PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE SEQRES 4 A 390 ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS SEQRES 5 A 390 HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY SEQRES 6 A 390 TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG SEQRES 7 A 390 HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL SEQRES 8 A 390 GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER SEQRES 9 A 390 ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL SEQRES 10 A 390 ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR SEQRES 11 A 390 GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN SEQRES 12 A 390 ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE SEQRES 13 A 390 GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SEQRES 14 A 390 SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU SEQRES 15 A 390 GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL SEQRES 16 A 390 GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN SEQRES 17 A 390 LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR SEQRES 18 A 390 ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP SEQRES 19 A 390 THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU SEQRES 20 A 390 ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO SEQRES 21 A 390 CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS SEQRES 22 A 390 GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY SEQRES 23 A 390 ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET SEQRES 24 A 390 GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP SEQRES 25 A 390 THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL SEQRES 26 A 390 SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU SEQRES 27 A 390 ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE SEQRES 28 A 390 GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER SEQRES 29 A 390 ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN SEQRES 30 A 390 LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU SEQRES 1 B 390 GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SEQRES 2 B 390 SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG SEQRES 3 B 390 PHE GLY GLU ALA ARG GLY ASN SER ALA PRO LEU ILE ILE SEQRES 4 B 390 ARG GLU PRO PHE ILE ALA CYS GLY PRO LYS GLU CYS LYS SEQRES 5 B 390 HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY SEQRES 6 B 390 TYR TYR ASN GLY THR ARG GLU ASP ARG ASN LYS LEU ARG SEQRES 7 B 390 HIS LEU ILE SER VAL LYS LEU GLY LYS ILE PRO THR VAL SEQRES 8 B 390 GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER SEQRES 9 B 390 ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL SEQRES 10 B 390 ASP GLY PRO ASP SER ASN ALA LEU ILE LYS ILE LYS TYR SEQRES 11 B 390 GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA ASN SEQRES 12 B 390 ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE SEQRES 13 B 390 GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SEQRES 14 B 390 SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU SEQRES 15 B 390 GLY ARG ILE ILE LYS GLU ILE PHE PRO THR GLY ARG VAL SEQRES 16 B 390 GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN SEQRES 17 B 390 LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR SEQRES 18 B 390 ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP SEQRES 19 B 390 THR ALA GLU ILE ARG LEU MET CYS THR GLU THR TYR LEU SEQRES 20 B 390 ASP THR PRO ARG PRO ASP ASP GLY SER ILE THR GLY PRO SEQRES 21 B 390 CYS GLU SER ASN GLY ASP LYS GLY ARG GLY GLY ILE LYS SEQRES 22 B 390 GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY SEQRES 23 B 390 ARG TRP TYR SER ARG THR MET SER LYS THR GLU ARG MET SEQRES 24 B 390 GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP SEQRES 25 B 390 THR ASP SER ASP ALA LEU ALA HIS SER GLY VAL MET VAL SEQRES 26 B 390 SER MET LYS GLU PRO GLY TRP TYR SER PHE GLY PHE GLU SEQRES 27 B 390 ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE SEQRES 28 B 390 GLU MET VAL HIS ASP GLY GLY LYS LYS THR TRP HIS SER SEQRES 29 B 390 ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN SEQRES 30 B 390 LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU MODRES 1NSB ASN A 283 ASN GLYCOSYLATION SITE MODRES 1NSB ASN B 283 ASN GLYCOSYLATION SITE FTNOTE 1 RESIDUES PRO A 138, PRO A 325, PRO B 138, AND PRO B 325 FTNOTE 1 ARE CIS PROLINES. HET NAG A 1 27 HET NAG B 1 27 HET CA A 2 1 HET CA B 2 1 HET CA 3 1 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM CA CALCIUM ION HETSYN NAG NAG FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 5 CA 3(CA 2+) FORMUL 8 HOH *446(H2 O) HELIX 1 1 SER A 98 GLY A 103 5 6 HELIX 2 2 PRO A 195 ASN A 198 5 4 HELIX 3 3 SER B 98 GLY B 103 5 6 HELIX 4 4 PRO B 195 ASN B 198 5 4 SHEET 1 1A 4 ILE A 113 CYS A 121 0 SHEET 2 1A 4 CYS A 126 THR A 132 -1 N LEU A 131 O ARG A 115 SHEET 3 1A 4 HIS A 154 LYS A 159 1 O VAL A 158 N HIS A 128 SHEET 4 1A 4 ILE A 170 ALA A 174 -1 O ILE A 170 N SER A 157 SHEET 1 2A 4 SER A 177 HIS A 182 0 SHEET 2 2A 4 TRP A 187 ASP A 193 -1 N VAL A 192 O SER A 177 SHEET 3 2A 4 LEU A 200 TYR A 205 1 N LYS A 202 O GLY A 191 SHEET 4 2A 4 ALA A 208 HIS A 214 -1 N TYR A 213 O ILE A 201 SHEET 1 3AA 4 ARG A 222 THR A 223 0 SHEET 2 3AA 4 ASP A 234 GLY A 242 -1 O THR A 240 N ARG A 222 SHEET 3 3AA 4 SER A 248 ARG A 256 1 N LEU A 253 O LEU A 237 SHEET 4 3AA 4 ARG A 259 ILE A 264 -1 N ARG A 259 O ARG A 256 SHEET 1 3BA 4 ASN A 229 ILE A 231 0 SHEET 2 3BA 4 ASP A 234 GLY A 242 -1 O TYR A 236 N ASN A 229 SHEET 3 3BA 4 SER A 248 ARG A 256 1 N LEU A 253 O LEU A 237 SHEET 4 3BA 4 ARG A 259 ILE A 264 -1 N ARG A 259 O ARG A 256 SHEET 1 4A 4 GLU A 274 PHE A 280 0 SHEET 2 4A 4 THR A 285 ARG A 291 -1 O ARG A 291 N GLU A 274 SHEET 3 4A 4 PRO A 300 ASN A 305 1 O PRO A 300 N CYS A 290 SHEET 4 4A 4 THR A 310 LEU A 315 -1 O THR A 310 N ASN A 305 SHEET 1 5A 4 PHE A 351 ARG A 355 0 SHEET 2 5A 4 ILE A 360 ARG A 366 -1 O TRP A 363 N VAL A 352 SHEET 3 5A 4 MET A 376 TYR A 382 1 N GLU A 377 O ARG A 366 SHEET 4 5A 4 ALA A 394 VAL A 400 -1 N ALA A 394 O VAL A 380 SHEET 1 6A 4 SER A 409 LYS A 415 0 SHEET 2 6A 4 ASP A 420 HIS A 430 -1 O GLY A 425 N PHE A 410 SHEET 3 6A 4 SER A 439 LEU A 447 1 O ALA A 443 N ILE A 426 SHEET 4 6A 4 PHE A 91 ILE A 97 -1 O ILE A 97 N THR A 442 SHEET 1 1B 4 ILE B 113 CYS B 121 0 SHEET 2 1B 4 CYS B 126 THR B 132 -1 N LEU B 131 O ARG B 115 SHEET 3 1B 4 HIS B 154 LYS B 159 1 O VAL B 158 N HIS B 128 SHEET 4 1B 4 ILE B 170 ALA B 174 -1 O ILE B 170 N SER B 157 SHEET 1 2B 4 SER B 177 HIS B 182 0 SHEET 2 2B 4 TRP B 187 ASP B 193 -1 N VAL B 192 O SER B 177 SHEET 3 2B 4 LEU B 200 TYR B 205 1 N LYS B 202 O GLY B 191 SHEET 4 2B 4 ALA B 208 HIS B 214 -1 N TYR B 213 O ILE B 201 SHEET 1 3AB 4 ARG B 222 THR B 223 0 SHEET 2 3AB 4 ASP B 234 GLY B 242 -1 O THR B 240 N ARG B 222 SHEET 3 3AB 4 SER B 248 ARG B 256 1 N LEU B 253 O LEU B 237 SHEET 4 3AB 4 ARG B 259 ILE B 264 -1 N ARG B 259 O ARG B 256 SHEET 1 3BB 4 ASN B 229 ILE B 231 0 SHEET 2 3BB 4 ASP B 234 GLY B 242 -1 O TYR B 236 N ASN B 229 SHEET 3 3BB 4 SER B 248 ARG B 256 1 N LEU B 253 O LEU B 237 SHEET 4 3BB 4 ARG B 259 ILE B 264 -1 N ARG B 259 O ARG B 256 SHEET 1 4B 4 GLU B 274 PHE B 280 0 SHEET 2 4B 4 THR B 285 ARG B 291 -1 O ARG B 291 N GLU B 274 SHEET 3 4B 4 PRO B 300 ASN B 305 1 O PRO B 300 N CYS B 290 SHEET 4 4B 4 THR B 310 LEU B 315 -1 O THR B 310 N ASN B 305 SHEET 1 5B 4 PHE B 351 ARG B 355 0 SHEET 2 5B 4 ILE B 360 ARG B 366 -1 O TRP B 363 N VAL B 352 SHEET 3 5B 4 MET B 376 TYR B 382 1 N GLU B 377 O ARG B 366 SHEET 4 5B 4 ALA B 394 VAL B 400 -1 N ALA B 394 O VAL B 380 SHEET 1 6B 4 SER B 409 LYS B 415 0 SHEET 2 6B 4 ASP B 420 HIS B 430 -1 O GLY B 425 N PHE B 410 SHEET 3 6B 4 SER B 439 LEU B 447 1 O ALA B 443 N ILE B 426 SHEET 4 6B 4 PHE B 91 ILE B 97 -1 O ILE B 97 N THR B 442 TURN 1 1A GLU A 104 GLY A 107 TURN 2 2A TYR A 142 THR A 145 TURN 3 3A LYS A 159 LYS A 162 TURNS IN SHEET STRAND B1L34 TURN 4 4A PRO A 195 ASN A 198 TURNS IN SHEET STRAND B2L23 TURN 5 5A TYR A 205 ALA A 208 TURNS IN SHEET STRAND B2L34 TURN 6 6A ILE A 231 ASP A 234 TURNS IN SHEET STRAND B3L12 TURN 7 7A SER A 243 GLY A 246 TURNS IN SHEET STRAND B3L23 TURN 8 8A ARG A 256 ARG A 259 TURNS IN SHEET STRAND B3L34 TURN 9 9A ASP A 328 SER A 331 TURN 10 10A PRO A 335 SER A 338 TURN 11 11A ASP A 385 THR A 388 TURNS IN SHEET STRAND B5L34 TURN 12 12A SER A 401 GLU A 404 TURN 13 13A GLY A 433 THR A 436 TURNS IN SHEET STRAND B6L23 TURN 14 14A ASP A 462 LEU A 465 TURN 15 1B GLU B 104 GLY B 107 TURN 16 2B TYR B 142 THR B 145 TURN 17 3B LYS B 159 LYS B 162 TURNS IN SHEET STRAND B1L34 TURN 18 4B PRO B 195 ASN B 198 TURNS IN SHEET STRAND B2L23 TURN 19 5B TYR B 205 ALA B 208 TURNS IN SHEET STRAND B2L34 TURN 20 6B ILE B 231 ASP B 234 TURNS IN SHEET STRAND B3L12 TURN 21 7B SER B 243 GLY B 246 TURNS IN SHEET STRAND B3L23 TURN 22 8B ARG B 256 ARG B 259 TURNS IN SHEET STRAND B3L34 TURN 23 9B ASP B 328 SER B 331 TURN 24 10B PRO B 335 SER B 338 TURN 25 11B ASP B 385 THR B 388 TURNS IN SHEET STRAND B5L34 TURN 26 12B SER B 401 GLU B 404 TURN 27 13B GLY B 433 THR B 436 TURNS IN SHEET STRAND B6L23 TURN 28 14B ASP B 462 LEU B 465 SSBOND 1 CYS A 86 CYS A 419 SSBOND 2 CYS A 121 CYS A 126 SSBOND 3 CYS A 181 CYS A 228 SSBOND 4 CYS A 230 CYS A 235 SSBOND 5 CYS A 276 CYS A 290 SSBOND 6 CYS A 278 CYS A 288 SSBOND 7 CYS A 317 CYS A 336 SSBOND 8 CYS A 423 CYS A 446 SSBOND 9 CYS B 86 CYS B 419 SSBOND 10 CYS B 121 CYS B 126 SSBOND 11 CYS B 181 CYS B 228 SSBOND 12 CYS B 230 CYS B 235 SSBOND 13 CYS B 276 CYS B 290 SSBOND 14 CYS B 278 CYS B 288 SSBOND 15 CYS B 317 CYS B 336 SSBOND 16 CYS B 423 CYS B 446 LINK ND2 ASN A 283 C1 NAG A 1 LINK ND2 ASN B 283 C1 NAG B 1 CISPEP 1 GLN A 137 PRO A 138 0 -7.82 CISPEP 2 THR A 324 PRO A 325 0 4.08 CISPEP 3 GLN B 137 PRO B 138 0 -2.30 CISPEP 4 THR B 324 PRO B 325 0 -1.30 SITE 1 CHA 5 ASP A 292 THR A 296 ASP A 323 GLY A 343 SITE 2 CHA 5 GLY A 345 SITE 1 CLA 1 GLU A 167 SITE 1 SIA 9 ARG A 115 ASP A 148 ARG A 149 TRP A 176 SITE 2 SIA 9 ILE A 220 ARG A 222 GLU A 274 ARG A 291 SITE 3 SIA 9 ASP A 323 SITE 1 CHB 5 ASP B 292 THR B 296 ASP B 323 GLY B 343 SITE 2 CHB 5 GLY B 345 SITE 1 CLB 1 GLU B 167 SITE 1 SIB 9 ARG B 115 ASP B 148 ARG B 149 TRP B 176 SITE 2 SIB 9 ILE B 220 ARG B 222 GLU B 274 ARG B 291 SITE 3 SIB 9 ASP B 323 CRYST1 88.900 88.900 222.800 90.00 90.00 120.00 P 31 2 1 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011249 0.006494 0.000000 0.00000 SCALE2 0.000000 0.012989 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004488 0.00000 MTRIX1 1 0.250000 0.433000 -0.866000 0.00000 1 MTRIX2 1 0.433000 0.750000 0.500000 0.00000 1 MTRIX3 1 0.866000 -0.500000 0.000000 0.00000 1